Crystal structures of apo and metal-bound forms of the UreE protein from Helicobacter pylori : role of multiple metal binding sites

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DOIResolve DOI: http://doi.org/10.1021/bi100372h
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TypeArticle
Journal titleBiochemistry
Volume49
Issue33
Pages70807088; # of pages: 9
AbstractThe crystal structure of the urease maturation protein UreE from Helicobacter pylori has been determined in its apo form at 2.1A ° resolution, bound to Cu2þ at 2.7A ° resolution, and bound to Ni2þ at 3.1A ° resolution. Apo UreE forms dimers, while the metal-bound enzymes are arranged as tetramers that consist of a dimer of dimers associated around the metal ion through coordination by His102 residues from each subunit of the tetramer. Comparison of independent subunits from different crystal forms indicates changes in the relative arrangement of the N- and C-terminal domains in response to metal binding. The improved ability of engineered versions of UreE containing hexahistidine sequences at either the N-terminal or C-terminal end to provide Ni2þ for the final metal sink (urease) is eliminated in the H102A version. Therefore, the ability of the improved Ni2þ-binding versions to deliver more nickel is likely an effect of an increased local concentration of metal ions that can rapidly replenish transferred ions bound to His102.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada (NRC-CNRC); NRC Biotechnology Research Institute
Peer reviewedYes
NRC number53123
NPARC number16526904
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Record identifier11aa7224-0e89-427b-b9ce-2741acbfcece
Record created2010-12-14
Record modified2016-05-09
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